메뉴 건너뛰기




Volumn 17, Issue 6, 2004, Pages 357-363

Cysteine protease cathepsin S as a key step in antigen presentation

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; CATHEPSIN S; CATHEPSIN S INHIBITOR; CHAPERONE; COLLAGEN; COLLAGEN ANTIBODY; CONCANAVALIN A; CYSTATIN C; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; FC RECEPTOR; GAMMA INTERFERON; INTERLEUKIN 1BETA; LOW DENSITY LIPOPROTEIN RECEPTOR; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; MYELIN BASIC PROTEIN; N MORPHOLINUREA LEUCINE HOMOPHENYLALANINE VINYLSULFONE PHENYL; OVALBUMIN; PAPAIN; UNCLASSIFIED DRUG;

EID: 4644335880     PISSN: 02140934     EISSN: None     Source Type: Journal    
DOI: 10.1358/dnp.2004.17.6.829027     Document Type: Review
Times cited : (30)

References (83)
  • 1
    • 0028038426 scopus 로고
    • MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation
    • Germain, R.N. MHC-dependent antigen processing and peptide presentation: Providing ligands for T lymphocyte activation. Cell 1994, 76: 287-99.
    • (1994) Cell , vol.76 , pp. 287-299
    • Germain, R.N.1
  • 2
    • 0021550018 scopus 로고
    • Antigen-presenting function of the macrophage
    • Unanue, E.R. Antigen-presenting function of the macrophage. Annu Rev Immunol 1984, 2: 395-428.
    • (1984) Annu Rev Immunol , vol.2 , pp. 395-428
    • Unanue, E.R.1
  • 3
    • 0033404624 scopus 로고    scopus 로고
    • Proteases involved in MHC class H antigen presentation
    • Villadangos, J.A., Bryant, R.A., Deussing, J. et al. Proteases involved in MHC class H antigen presentation. Immunol Rev 1999, 172: 109-20.
    • (1999) Immunol Rev , vol.172 , pp. 109-120
    • Villadangos, J.A.1    Bryant, R.A.2    Deussing, J.3
  • 4
    • 0033966413 scopus 로고    scopus 로고
    • Cathepsins and compartmentalization in antigen presentation
    • Riese, R.J. and Chapman, H.A. Cathepsins and compartmentalization in antigen presentation. Curr Opin Immunol 2000, 12: 107-13.
    • (2000) Curr Opin Immunol , vol.12 , pp. 107-113
    • Riese, R.J.1    Chapman, H.A.2
  • 5
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: Facts and opportunities
    • Turk, V., Turk, B. and Turk, D. Lysosomal cysteine proteases: Facts and opportunities. EMBO J 2001, 20: 4629-33.
    • (2001) EMBO J , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 6
    • 0033430264 scopus 로고    scopus 로고
    • The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation
    • Nakagawa, T.Y. and Rudensky, A.Y. The role of lysosomal proteinases in MHC class II-mediated antigen processing and presentation. Immunol Rev 1999, 172: 121-9.
    • (1999) Immunol Rev , vol.172 , pp. 121-129
    • Nakagawa, T.Y.1    Rudensky, A.Y.2
  • 7
    • 0032986028 scopus 로고    scopus 로고
    • The lysosomal cysteine proteases
    • McGrath, M.E. The lysosomal cysteine proteases. Annu Rev Biophys Struct 1999, 28: 181-204.
    • (1999) Annu Rev Biophys Struct , vol.28 , pp. 181-204
    • McGrath, M.E.1
  • 8
    • 0037459360 scopus 로고    scopus 로고
    • Deficiency of the cysteine protease cathepsin S impairs microvessel growth
    • Shi, G.P., Sukhova, G.K., Kuzuya, M. et al. Deficiency of the cysteine protease cathepsin S impairs microvessel growth. Circ Res 2003, 92: 493-500.
    • (2003) Circ Res , vol.92 , pp. 493-500
    • Shi, G.P.1    Sukhova, G.K.2    Kuzuya, M.3
  • 9
    • 0037362831 scopus 로고    scopus 로고
    • Deficiency of cathepsin S reduces atherosclerosis in LDL receptor-deficient mice
    • Sukhova, G.K., Zhang, Y., Pan, J.H. et al. Deficiency of cathepsin S reduces atherosclerosis in LDL receptor-deficient mice. J Clin Invest 2003, 111: 897-906.
    • (2003) J Clin Invest , vol.111 , pp. 897-906
    • Sukhova, G.K.1    Zhang, Y.2    Pan, J.H.3
  • 10
    • 0036661021 scopus 로고    scopus 로고
    • Apoptotic pathways: Involvement of lysosomal proteases
    • Turk, B., Stoka, V., Rozman-Pungercar, J. et al. Apoptotic pathways: Involvement of lysosomal proteases. Biol Chem 2002, 383: 1035-44.
    • (2002) Biol Chem , vol.383 , pp. 1035-1044
    • Turk, B.1    Stoka, V.2    Rozman-Pungercar, J.3
  • 11
    • 0030970119 scopus 로고    scopus 로고
    • Emerging roles for cysteine proteases in human biology
    • Chapman, H.A., Riese, R.J. and Shi, G.P. Emerging roles for cysteine proteases in human biology. Annu Rev Physiol 1997, 59: 63-88.
    • (1997) Annu Rev Physiol , vol.59 , pp. 63-88
    • Chapman, H.A.1    Riese, R.J.2    Shi, G.P.3
  • 12
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R.J., Wolf, P.R., Bromme, D. et al. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 1996, 4: 357-66.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Bromme, D.3
  • 13
    • 0016776255 scopus 로고
    • Acid sulfhydryl protease from calf lymph nodes
    • Tumsek, T., Kregar, I. and Lebez, D. Acid sulfhydryl protease from calf lymph nodes. Biochim Biophys Acta 1975, 403: 514-20.
    • (1975) Biochim Biophys Acta , vol.403 , pp. 514-520
    • Tumsek, T.1    Kregar, I.2    Lebez, D.3
  • 14
    • 0026770758 scopus 로고
    • Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S
    • Wiederanders, B., Brömme, D., Kirschke, H. et al. Phylogenetic conservation of cysteine proteinases. Cloning and expression of a cDNA coding for human cathepsin S. J Biol Chem 1992, 267: 13708-13.
    • (1992) J Biol Chem , vol.267 , pp. 13708-13713
    • Wiederanders, B.1    Brömme, D.2    Kirschke, H.3
  • 15
    • 0026630108 scopus 로고
    • Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease
    • Shi, G.-P., Munger, J.S., Meara, J.P. et al. Molecular cloning and expression of human alveolar macrophage cathepsin S, an elastinolytic cysteine protease. J Biol Chem 1992, 267: 7258-62.
    • (1992) J Biol Chem , vol.267 , pp. 7258-7262
    • Shi, G.-P.1    Munger, J.S.2    Meara, J.P.3
  • 16
    • 0028245277 scopus 로고
    • Human cathepsin S: Chromosomal localization, gene structure and tissue distribution
    • Shi, G.P., Webb, A.C., Foster, K.E. et al. Human cathepsin S: Chromosomal localization, gene structure and tissue distribution. J Biol Chem 1994, 269: 11530-6.
    • (1994) J Biol Chem , vol.269 , pp. 11530-11536
    • Shi, G.P.1    Webb, A.C.2    Foster, K.E.3
  • 17
    • 0030890614 scopus 로고    scopus 로고
    • Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes
    • Linnevers, C., Smeekens, S.P. and Brömme, D. Human cathepsin W, a putative cysteine protease predominantly expressed in CD8+ T-lymphocytes. FEBS Lett 1997, 405: 253-9.
    • (1997) FEBS Lett , vol.405 , pp. 253-259
    • Linnevers, C.1    Smeekens, S.P.2    Brömme, D.3
  • 18
    • 0035143028 scopus 로고    scopus 로고
    • Expression patterns of cathepsins B, H, K, L and S in the human endometrium
    • Jokimaa, V., Oksjoki, S., Kujari, H. et al. Expression patterns of cathepsins B, H, K, L and S in the human endometrium. Mol Hum Reprod 2001, 7: 73-8.
    • (2001) Mol Hum Reprod , vol.7 , pp. 73-78
    • Jokimaa, V.1    Oksjoki, S.2    Kujari, H.3
  • 19
    • 0034796148 scopus 로고    scopus 로고
    • Expression of cathepsin B, L, S and D by gastric epithelial cells implicates them as antigen presenting cells in local immune responses
    • Barrera, C., Ye, G., Espejo, R. et al. Expression of cathepsin B, L, S and D by gastric epithelial cells implicates them as antigen presenting cells in local immune responses. Hum Immunol 2001, 62: 1081-91.
    • (2001) Hum Immunol , vol.62 , pp. 1081-1091
    • Barrera, C.1    Ye, G.2    Espejo, R.3
  • 20
    • 0036158627 scopus 로고    scopus 로고
    • CST3 genotype associated with exudative age related macular degeneration
    • Zurdel, J., Finckh, U., Menzer, G. et al. CST3 genotype associated with exudative age related macular degeneration. Br J Ophthalmol 2002, 86: 214-9.
    • (2002) Br J Ophthalmol , vol.86 , pp. 214-219
    • Zurdel, J.1    Finckh, U.2    Menzer, G.3
  • 21
    • 0028206592 scopus 로고
    • Differential distribution of messenger RNAs for cathepsins B, L and S in adult rat brain: An in situ hybridization study
    • Petanceska, S., Bruke, S., Watson, S.J. et al. Differential distribution of messenger RNAs for cathepsins B, L and S in adult rat brain: An in situ hybridization study. Neuroscience 1994, 59: 728-39.
    • (1994) Neuroscience , vol.59 , pp. 728-739
    • Petanceska, S.1    Bruke, S.2    Watson, S.J.3
  • 22
    • 0037308679 scopus 로고    scopus 로고
    • Activity and subcellular distribution of cathepsin in primary human monocytes
    • Greiner, A., Lautwein, A., Overkleeft, H.S. et al. Activity and subcellular distribution of cathepsin in primary human monocytes. J Leukoc Biol 2003, 73: 235-42.
    • (2003) J Leukoc Biol , vol.73 , pp. 235-242
    • Greiner, A.1    Lautwein, A.2    Overkleeft, H.S.3
  • 23
    • 0031736958 scopus 로고    scopus 로고
    • Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics
    • Fengler, A. and Brandt, W. Three-dimensional structures of the cysteine proteases cathepsins K and S deduced by knowledge-based modelling and active site characteristics. Protein Eng 1998, 11: 1007-13.
    • (1998) Protein Eng , vol.11 , pp. 1007-1013
    • Fengler, A.1    Brandt, W.2
  • 24
    • 0031746634 scopus 로고    scopus 로고
    • Crystal structure of human cathepsin S
    • McGrath, M.E., Palmer, J.T., Bromme, D. et al. Crystal structure of human cathepsin S. Protein Sci 1998, 7: 1294-302.
    • (1998) Protein Sci , vol.7 , pp. 1294-1302
    • McGrath, M.E.1    Palmer, J.T.2    Bromme, D.3
  • 25
    • 0037028023 scopus 로고    scopus 로고
    • Design and synthesis of dipeptide nitriles as reversible and potent cathepsin S inhibitors
    • Ward, Y.D., Thomson, D.S., Frye, L.L. et al. Design and synthesis of dipeptide nitriles as reversible and potent cathepsin S inhibitors. J Med Chem 2002, 45: 5471-82.
    • (2002) J Med Chem , vol.45 , pp. 5471-5482
    • Ward, Y.D.1    Thomson, D.S.2    Frye, L.L.3
  • 26
  • 27
    • 0037465823 scopus 로고    scopus 로고
    • Specificity determinants of human cathepsin S revealed by crystal structures of complexes
    • Pauly, T.A., Sulea, T., Ammirati, M. et al. Specificity determinants of human cathepsin S revealed by crystal structures of complexes. Biochemistry 2003, 42: 3203-13.
    • (2003) Biochemistry , vol.42 , pp. 3203-3213
    • Pauly, T.A.1    Sulea, T.2    Ammirati, M.3
  • 28
    • 0034628448 scopus 로고    scopus 로고
    • Protease inhibitors: Current status and future prospects
    • Leung, D., Abbenante, G. and Fairlie, D.P. Protease inhibitors: Current status and future prospects. J Med Chem 2000, 43: 305-41.
    • (2000) J Med Chem , vol.43 , pp. 305-341
    • Leung, D.1    Abbenante, G.2    Fairlie, D.P.3
  • 29
    • 0027469584 scopus 로고
    • Functional expression of human cathepsin S in saccharomyces cerevisiae
    • Brömme, D., Bonneau, P.R., Lachance, P. et al. Functional expression of human cathepsin S in saccharomyces cerevisiae. J Biol Chem 1993, 286: 4832-8.
    • (1993) J Biol Chem , vol.286 , pp. 4832-4838
    • Brömme, D.1    Bonneau, P.R.2    Lachance, P.3
  • 31
    • 0024818636 scopus 로고
    • The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsin L and B
    • Brömme, D., Steinert, A., Friebe, S. et al. The specificity of bovine spleen cathepsin S. A comparison with rat liver cathepsin L and B. Biochem J 1989, 264: 475-81.
    • (1989) Biochem J , vol.264 , pp. 475-481
    • Brömme, D.1    Steinert, A.2    Friebe, S.3
  • 32
    • 0027050951 scopus 로고
    • The specificity and elastinolytic activities of bovine cathepsins S and H
    • Xin, X.Q., Gunesekera, B. and Mason, R.W. The specificity and elastinolytic activities of bovine cathepsins S and H. Arch Biochem Biophys 1992, 299: 334-9.
    • (1992) Arch Biochem Biophys , vol.299 , pp. 334-339
    • Xin, X.Q.1    Gunesekera, B.2    Mason, R.W.3
  • 33
    • 0035666656 scopus 로고    scopus 로고
    • Cathepsin S and asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro
    • Beck, H., Schwarz, G. Schroter, C.J. et al. Cathepsin S and asparagine-specific endoprotease dominate the proteolytic processing of human myelin basic protein in vitro. Eur J Immunol 2001, 31: 3726-36.
    • (2001) Eur J Immunol , vol.31 , pp. 3726-3736
    • Beck, H.1    Schwarz, G.2    Schroter, C.J.3
  • 34
    • 0029931108 scopus 로고    scopus 로고
    • Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading
    • Riese, R.J., Wolf, P.R., Brömme, D. et al. Essential role for cathepsin S in MHC class II-associated invariant chain processing and peptide loading. Immunity 1996, 4: 357-66.
    • (1996) Immunity , vol.4 , pp. 357-366
    • Riese, R.J.1    Wolf, P.R.2    Brömme, D.3
  • 35
    • 0026557924 scopus 로고
    • Chemistry and functional role of the invariant chain
    • Cresswell, P. Chemistry and functional role of the invariant chain. Curr Opin Immunol 1992, 4: 87-92.
    • (1992) Curr Opin Immunol , vol.4 , pp. 87-92
    • Cresswell, P.1
  • 36
    • 0027303736 scopus 로고
    • Peptide binding inhibits protein aggregation of invariant-chain free class II dimmers and promotes surface expression of occupied molecules
    • Germain, R.N. and Rinker, A.G. Peptide binding inhibits protein aggregation of invariant-chain free class II dimmers and promotes surface expression of occupied molecules. Nature 1993, 363: 275-8.
    • (1993) Nature , vol.363 , pp. 275-278
    • Germain, R.N.1    Rinker, A.G.2
  • 37
    • 0025602116 scopus 로고
    • Intracellular transport of class II MHC molecules directed by invariant chain
    • Lotteau, V., Teyton, L., Peleraux, A. et al. Intracellular transport of class II MHC molecules directed by invariant chain. Nature 1990, 348: 600-5.
    • (1990) Nature , vol.348 , pp. 600-605
    • Lotteau, V.1    Teyton, L.2    Peleraux, A.3
  • 38
    • 0025202076 scopus 로고
    • MHC class II-associated invariant chain contains a sorting signal for endosomal compartments
    • Bakke, O. and Dobberstein, B. MHC class II-associated invariant chain contains a sorting signal for endosomal compartments. Cell 1990, 63: 707-16.
    • (1990) Cell , vol.63 , pp. 707-716
    • Bakke, O.1    Dobberstein, B.2
  • 39
    • 0028981178 scopus 로고
    • HLA-DM induces CLIP dissociation from MHC class II alpha-beta dimmers and facilitates peptide loading
    • Denzin, L.K. and Cresswell, P. HLA-DM induces CLIP dissociation from MHC class II alpha-beta dimmers and facilitates peptide loading. Cell 1995, 82: 155-65.
    • (1995) Cell , vol.82 , pp. 155-165
    • Denzin, L.K.1    Cresswell, P.2
  • 40
    • 0141832121 scopus 로고    scopus 로고
    • MHC-guided processing binding of large antigen fragments
    • Sercarz, E.E. and Maverakis, E. MHC-guided processing binding of large antigen fragments. Nat Rev Immunol 2003, 3: 621-9.
    • (2003) Nat Rev Immunol , vol.3 , pp. 621-629
    • Sercarz, E.E.1    Maverakis, E.2
  • 41
    • 0036227429 scopus 로고    scopus 로고
    • Diversity in MHC class II antigen presentation
    • Robinson, J.H. and Delvig, A.A. Diversity in MHC class II antigen presentation. Immunology 2002, 105: 252-62.
    • (2002) Immunology , vol.105 , pp. 252-262
    • Robinson, J.H.1    Delvig, A.A.2
  • 42
    • 0032103322 scopus 로고    scopus 로고
    • Cathepsin S activity regulates antigen presentation and immunity
    • Riese, R.J., Mitchell, R.N., Valladangos, J.A. et al. Cathepsin S activity regulates antigen presentation and immunity. J Clin Invest 1998, 101: 2351-63.
    • (1998) J Clin Invest , vol.101 , pp. 2351-2363
    • Riese, R.J.1    Mitchell, R.N.2    Valladangos, J.A.3
  • 43
    • 0030790341 scopus 로고    scopus 로고
    • Degradation of mouse invariant chain: Roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism
    • Villadangos, J.A., Riese, R.J., Peters, C. et al. Degradation of mouse invariant chain: Roles of cathepsins S and D and the influence of major histocompatibility complex polymorphism. J Exp Med 1997, 186: 549-60.
    • (1997) J Exp Med , vol.186 , pp. 549-560
    • Villadangos, J.A.1    Riese, R.J.2    Peters, C.3
  • 44
    • 0032516003 scopus 로고    scopus 로고
    • Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
    • Deussing, J., Roth, W., Saftig, P. et al. Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc Natl Acad Sci USA 1998, 95: 4516-21.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 4516-4521
    • Deussing, J.1    Roth, W.2    Saftig, P.3
  • 45
    • 0033083688 scopus 로고    scopus 로고
    • Cathepsin S required for normal MHC class II peptide loading and germinal center development
    • Shi, G.P., Villadangos, J.A., Dranoff, G. et al. Cathepsin S required for normal MHC class II peptide loading and germinal center development. Immunity 1999, 10: 197-206.
    • (1999) Immunity , vol.10 , pp. 197-206
    • Shi, G.P.1    Villadangos, J.A.2    Dranoff, G.3
  • 46
    • 2442549710 scopus 로고    scopus 로고
    • Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice
    • Nakagawa, T.Y., Brissette, W.H., Lira, P.D. et al. Impaired invariant chain degradation and antigen presentation and diminished collagen-induced arthritis in cathepsin S null mice. Immunity 1999, 10: 207-17.
    • (1999) Immunity , vol.10 , pp. 207-217
    • Nakagawa, T.Y.1    Brissette, W.H.2    Lira, P.D.3
  • 47
    • 0032540474 scopus 로고    scopus 로고
    • Cathepsin L: Critical role in Ii degradation and CD4 T cell selection in the thymus
    • Nakagawa, T., Roth, W., Wong, P. et al. Cathepsin L: Critical role in Ii degradation and CD4 T cell selection in the thymus. Science 1998, 280: 450-3.
    • (1998) Science , vol.280 , pp. 450-453
    • Nakagawa, T.1    Roth, W.2    Wong, P.3
  • 48
    • 0033404624 scopus 로고    scopus 로고
    • Proteases involved in MHC class II antigen presentation
    • Villadangos, J.A., Bryant, R.A.R., Deussing, J. et al. Proteases involved in MHC class II antigen presentation. Immunol Rev 1999, 172: 109-20.
    • (1999) Immunol Rev , vol.172 , pp. 109-120
    • Villadangos, J.A.1    Bryant, R.A.R.2    Deussing, J.3
  • 49
    • 0034599498 scopus 로고    scopus 로고
    • Role for cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages
    • Shi, G.P., Bryant, A.R., Riese, R. et al. Role for Cathepsin F in invariant chain processing and major histocompatibility complex class II peptide loading by macrophages. J Exp Med 2000, 191: 1177-85.
    • (2000) J Exp Med , vol.191 , pp. 1177-1185
    • Shi, G.P.1    Bryant, A.R.2    Riese, R.3
  • 50
    • 0032546352 scopus 로고    scopus 로고
    • Dendritic cells and the control of immunity
    • Banchereau, J. and Steinman, R.M. Dendritic cells and the control of immunity. Nature 1998, 392: 245-52.
    • (1998) Nature , vol.392 , pp. 245-252
    • Banchereau, J.1    Steinman, R.M.2
  • 51
    • 0033571691 scopus 로고    scopus 로고
    • Cathepsin S controls the trafficking and maturation of MHC class II molecules in dendritic cells
    • Driesen, C., Bryant, R.A.R., Lennon-Dumenil, A.M. et al. Cathepsin S controls the trafficking and maturation of MHC class II molecules in dendritic cells. J Cell Biol 1999, 147: 775-90.
    • (1999) J Cell Biol , vol.147 , pp. 775-790
    • Driesen, C.1    Bryant, R.A.R.2    Lennon-Dumenil, A.M.3
  • 52
    • 0032568806 scopus 로고    scopus 로고
    • Development regulation of variant chain proteolysis controls MHC class II trafficking in mouse dendritic cells
    • Pierre, P. and Mellman, I. Development regulation of variant chain proteolysis controls MHC class II trafficking in mouse dendritic cells. Cell 1998, 93: 1135-45.
    • (1998) Cell , vol.93 , pp. 1135-1145
    • Pierre, P.1    Mellman, I.2
  • 53
    • 0034954037 scopus 로고    scopus 로고
    • MHC class II expression is regulated in dendritic cells independently of variant chain degradation
    • Villadangos, J.A., Cardoso, M., Steptoe, R.J. et al. MHC class II expression is regulated in dendritic cells independently of variant chain degradation. Immunity 2001, 14: 739-49.
    • (2001) Immunity , vol.14 , pp. 739-749
    • Villadangos, J.A.1    Cardoso, M.2    Steptoe, R.J.3
  • 54
    • 0038651151 scopus 로고    scopus 로고
    • Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs
    • Bania, J., Gatti, E., Lelouard, H. et al. Human cathepsin S, but not cathepsin L, degrades efficiently MHC class II-associated invariant chain in nonprofessional APCs. Proc Natl Acad Sci USA 2003, 100: 6664-9.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 6664-6669
    • Bania, J.1    Gatti, E.2    Lelouard, H.3
  • 55
    • 0034964922 scopus 로고    scopus 로고
    • Immunocompetent astrocytes and microglia display major differences in the processing of the variant chain in the expression of active cathepsin L and cathepsin S
    • Gresser, O., Weber, E., Hellwig, A. et al. Immunocompetent astrocytes and microglia display major differences in the processing of the variant chain in the expression of active cathepsin L and cathepsin S. Eur J Immunol 2001, 31: 1813-24.
    • (2001) Eur J Immunol , vol.31 , pp. 1813-1824
    • Gresser, O.1    Weber, E.2    Hellwig, A.3
  • 56
    • 20244366658 scopus 로고    scopus 로고
    • Antigen processing and presentation in human muscle: Cathepsin S is critical for MHC class II expression and upregulated in inflammatory myopathies
    • Wiendl, H., Lautwein, A., Mitsdorffer, M. et al. Antigen processing and presentation in human muscle: Cathepsin S is critical for MHC class II expression and upregulated in inflammatory myopathies. J Neuroimmunol 2003, 138: 132-43.
    • (2003) J Neuroimmunol , vol.138 , pp. 132-143
    • Wiendl, H.1    Lautwein, A.2    Mitsdorffer, M.3
  • 57
    • 0343867197 scopus 로고    scopus 로고
    • Individual cathepsins degrade immune complexes internalized by antigen-presenting cells via Fc gamma receptors
    • Driessen, D., Lennon-Duménil, A.-M. and Ploegh, H.L. Individual cathepsins degrade immune complexes internalized by antigen-presenting cells via Fc gamma receptors. Eur J Immunol 2001, 31: 1592-601.
    • (2001) Eur J Immunol , vol.31 , pp. 1592-1601
    • Driessen, D.1    Lennon-Duménil, A.-M.2    Ploegh, H.L.3
  • 58
    • 0036177422 scopus 로고    scopus 로고
    • Specific role for cathepsin S in the generation of antigenic peptides in vivo
    • Plüger, E.B., Boes, M., Alfonso, C. et al. Specific role for cathepsin S in the generation of antigenic peptides in vivo. Eur J Immunol 2002, 32: 467-76.
    • (2002) Eur J Immunol , vol.32 , pp. 467-476
    • Plüger, E.B.1    Boes, M.2    Alfonso, C.3
  • 59
    • 0037087364 scopus 로고    scopus 로고
    • A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation
    • Hsieh, C.-S., deRoos, P., Honey, K. et al. A role for cathepsin L and cathepsin S in peptide generation for MHC class II presentation. J Immunol 2002, 168: 2618-25.
    • (2002) J Immunol , vol.168 , pp. 2618-2625
    • Hsieh, C.-S.1    DeRoos, P.2    Honey, K.3
  • 60
    • 84888939261 scopus 로고    scopus 로고
    • Reversible cathepsin S (Cat S) inhibitors block invariant chain processing in vitro and reduced the severity of collagen-induced arthritis (CIA) in vivo
    • Allen, E., Vitali, N., Underwood, S. et al. Reversible cathepsin S (Cat S) inhibitors block invariant chain processing in vitro and reduced the severity of collagen-induced arthritis (CIA) in vivo. Inflamm Res 2002, 51(Suppl 2): S121, A1.
    • (2002) Inflamm Res , vol.51 , Issue.SUPPL. 2
    • Allen, E.1    Vitali, N.2    Underwood, S.3
  • 61
    • 0030961031 scopus 로고    scopus 로고
    • Recognition of the immunodominant myelin basic protein peptide by autoantibodies and HLA-DR2-restricted T cell clones from multiple sclerosis patients. Identity of key contact residues in the B-cell and T-cell epitopes
    • Wucherpfenning, K.W., Catz, I., Hausmann, S. et al. Recognition of the immunodominant myelin basic protein peptide by autoantibodies and HLA-DR2-restricted T cell clones from multiple sclerosis patients. Identity of key contact residues in the B-cell and T-cell epitopes. J Clin Invest 1997, 100: 1114-22.
    • (1997) J Clin Invest , vol.100 , pp. 1114-1122
    • Wucherpfenning, K.W.1    Catz, I.2    Hausmann, S.3
  • 62
    • 0032783985 scopus 로고    scopus 로고
    • Neurotrophic factors regulate cathepsin S in macrophages and microglia: A role in the degradation of myelin basic protein and amyloid beta peptide
    • Liuzzo, J.P., Pentaceska, S.S. and Devi, L.A. Neurotrophic factors regulate cathepsin S in macrophages and microglia: A role in the degradation of myelin basic protein and amyloid beta peptide. Mol Med 1999, 5: 334-43.
    • (1999) Mol Med , vol.5 , pp. 334-343
    • Liuzzo, J.P.1    Pentaceska, S.S.2    Devi, L.A.3
  • 63
    • 4644243201 scopus 로고    scopus 로고
    • Modulation of experimental autoimmune encephalomyelitis (EAE) by a non-peptide inhibitor for cathepsin S
    • Abst A5
    • Davis, G. and Jeij, I. Modulation of experimental autoimmune encephalomyelitis (EAE) by a non-peptide inhibitor for cathepsin S. Inflamm Res 2002, 51(Suppl 2): Abst A5.
    • (2002) Inflamm Res , vol.51 , Issue.SUPPL. 2
    • Davis, G.1    Jeij, I.2
  • 64
    • 18644380025 scopus 로고    scopus 로고
    • Cathepsin S activity is detectable in human keratinocytes and is selectively upregulated upon stimulation with interferon-gamma
    • Schwarz, G., Boehncke, W.H., Braun, M. et al. Cathepsin S activity is detectable in human keratinocytes and is selectively upregulated upon stimulation with interferon-gamma. J Invest Dermatol 2002, 119: 44-9.
    • (2002) J Invest Dermatol , vol.119 , pp. 44-49
    • Schwarz, G.1    Boehncke, W.H.2    Braun, M.3
  • 65
    • 0032465258 scopus 로고    scopus 로고
    • Identification and quantitation of interferon-gamma producing T cells in psoriatic lesions: Localization of both CD4+ and CD8+ subsets
    • Szabo, S.K., Hammerberg, C., Yoshida, Y. et al. Identification and quantitation of interferon-gamma producing T cells in psoriatic lesions: Localization of both CD4+ and CD8+ subsets. J Invest Dermatol 1998, 111: 1072-8.
    • (1998) J Invest Dermatol , vol.111 , pp. 1072-1078
    • Szabo, S.K.1    Hammerberg, C.2    Yoshida, Y.3
  • 66
    • 0028206592 scopus 로고
    • Differential distribution of messenger RNAs for cathepsins B, L and S in adult rat brain: An in situ hybridization study
    • Petanceska, S., Burke, S., Watson, S.J. et al. Differential distribution of messenger RNAs for cathepsins B, L and S in adult rat brain: An in situ hybridization study. Neuroscience 1994, 59: 729-38.
    • (1994) Neuroscience , vol.59 , pp. 729-738
    • Petanceska, S.1    Burke, S.2    Watson, S.J.3
  • 67
    • 0028927279 scopus 로고
    • The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. An immunocytochemical study
    • Lemere, C.A., Munger, J.S., Shi, G.P. et al. The lysosomal cysteine protease, cathepsin S, is increased in Alzheimer's disease and Down syndrome brain. An immunocytochemical study. Am J Pathol 1995, 146: 848-60.
    • (1995) Am J Pathol , vol.146 , pp. 848-860
    • Lemere, C.A.1    Munger, J.S.2    Shi, G.P.3
  • 68
    • 0029112811 scopus 로고
    • Lysosomal processing of amyloid precursor protein to Abeta peptides: A distinct role for cathepsin S
    • Munger, J.S., Haass, C., Lemere, C.A. et al. Lysosomal processing of amyloid precursor protein to Abeta peptides: A distinct role for cathepsin S. Biochem J 1995, 311: 290-305.
    • (1995) Biochem J , vol.311 , pp. 290-305
    • Munger, J.S.1    Haass, C.2    Lemere, C.A.3
  • 69
    • 0036329099 scopus 로고    scopus 로고
    • Cathepsins S inhibitor prevents autoantigen presentation and autoimmunity
    • Saegusa, K., Ishimaru, N., Yanagi, K. et al. Cathepsins S inhibitor prevents autoantigen presentation and autoimmunity. J Clin Invest 2002, 110: 361-9.
    • (2002) J Clin Invest , vol.110 , pp. 361-369
    • Saegusa, K.1    Ishimaru, N.2    Yanagi, K.3
  • 70
    • 84888979548 scopus 로고    scopus 로고
    • Use of 1-(piperazin-1-yl) alkyl-3-phenylpyrazole cathepsin S inhibitors in methods of treating allergies. PCT Int Appl 2002, WO 0220013
    • Cai, H., Edwards, J.P., Gu, Y. et al. Use of 1-(piperazin-1-yl) alkyl-3-phenylpyrazole cathepsin S inhibitors in methods of treating allergies. PCT Int Appl 2002, WO 0220013.
    • Cai, H.1    Edwards, J.P.2    Gu, Y.3
  • 71
    • 0038514893 scopus 로고    scopus 로고
    • Cathepsin S inhibitors block invariant chain processing and antigen-induced proliferation in vitro, and inhibit murine collagen-induced arthritis (CIA) and rat ovalbumin-induced asthma in vivo
    • Podolin, P.L., Capper, E.A., Bolognese, B.J. et al. Cathepsin S inhibitors block invariant chain processing and antigen-induced proliferation in vitro, and inhibit murine collagen-induced arthritis (CIA) and rat ovalbumin-induced asthma in vivo. Inflamm Res 2002, 51(Suppl 2): S133, A76.
    • (2002) Inflamm Res , vol.51 , Issue.SUPPL. 2
    • Podolin, P.L.1    Capper, E.A.2    Bolognese, B.J.3
  • 72
    • 0034812772 scopus 로고    scopus 로고
    • Circadian and concentration profile of cathepsin S in sera from healthy subjects and asthmatic patients
    • Cimerman, N., Brguljan, P.M., Krasovec, M. et al. Circadian and concentration profile of cathepsin S in sera from healthy subjects and asthmatic patients. Pflügers Arch 2001, 442(6 Suppl 1): R204-6.
    • (2001) Pflügers Arch , vol.442 , Issue.6 SUPPL. 1
    • Cimerman, N.1    Brguljan, P.M.2    Krasovec, M.3
  • 73
    • 0141961518 scopus 로고    scopus 로고
    • Therapy for chronic obstructive pulmonary disease in the 21st century
    • Donnelly, L.E. and Rogers, D.F. Therapy for chronic obstructive pulmonary disease in the 21st century. Drugs 2003, 63: 1973-8.
    • (2003) Drugs , vol.63 , pp. 1973-1978
    • Donnelly, L.E.1    Rogers, D.F.2
  • 74
    • 0036545472 scopus 로고    scopus 로고
    • Proteinase in chronic obstructive pulmonary disease
    • Shapiro, S.D. Proteinase in chronic obstructive pulmonary disease. Biochem Soc Trans 2001, 30: 98-102.
    • (2001) Biochem Soc Trans , vol.30 , pp. 98-102
    • Shapiro, S.D.1
  • 75
    • 0035915811 scopus 로고    scopus 로고
    • Expression of cathepsin B and S in the progression of prostate carcinoma
    • Fernandez, P.L., Farre, X., Nadal, A. et al. Expression of cathepsin B and S in the progression of prostate carcinoma. Int J Cancer 2001, 95: 51-5.
    • (2001) Int J Cancer , vol.95 , pp. 51-55
    • Fernandez, P.L.1    Farre, X.2    Nadal, A.3
  • 76
    • 0035914268 scopus 로고    scopus 로고
    • Cathepsin S in tumours, regional lymph nodes and sera of patients with lung cancer: Relation to prognosis
    • Kos, J., Sekimik, A., Kopitar, G. et al. Cathepsin S in tumours, regional lymph nodes and sera of patients with lung cancer: Relation to prognosis. Br J Cancer 2001, 85: 1193-200.
    • (2001) Br J Cancer , vol.85 , pp. 1193-1200
    • Kos, J.1    Sekimik, A.2    Kopitar, G.3
  • 77
    • 0032145836 scopus 로고    scopus 로고
    • Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells
    • Sukhova, G.K., Shi, G.-P. Simon, D.I. et al. Expression of the elastolytic cathepsins S and K in human atheroma and regulation of their production in smooth muscle cells. J Clin Invest 1998, 102: 576-83.
    • (1998) J Clin Invest , vol.102 , pp. 576-583
    • Sukhova, G.K.1    Shi, G.-P.2    Simon, D.I.3
  • 78
    • 84888980282 scopus 로고    scopus 로고
    • A role for cathepsin in atherosclerosis
    • Fos, J.H., Burns-Kurtis, C.L., Needle, S. et al. A role for cathepsin in atherosclerosis. Inflamm Res 2002, 51(Suppl 2): S130, A57.
    • (2002) Inflamm Res , vol.51 , Issue.SUPPL. 2
    • Fos, J.H.1    Burns-Kurtis, C.L.2    Needle, S.3
  • 79
    • 0034773298 scopus 로고    scopus 로고
    • Presentation of antigens by MHC class II molecules: Getting the most out of them
    • Villadangos, J.A. Presentation of antigens by MHC class II molecules: Getting the most out of them. Mol Immunol 2001, 38: 329-46.
    • (2001) Mol Immunol , vol.38 , pp. 329-346
    • Villadangos, J.A.1
  • 80
    • 0037805704 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases regulate antigen presentation
    • Honey, K. and Rodensky, A.Y. Lysosomal cysteine proteases regulate antigen presentation. Nat Rev Immunol 2003, 3: 472-82.
    • (2003) Nat Rev Immunol , vol.3 , pp. 472-482
    • Honey, K.1    Rodensky, A.Y.2
  • 81
    • 0036119488 scopus 로고    scopus 로고
    • Recent developments of cathepsin inhibitors and their selectivity
    • Kim, W. and Kang, K. Recent developments of cathepsin inhibitors and their selectivity. Expert Opin Ther Patents 2002, 12: 419-32.
    • (2002) Expert Opin Ther Patents , vol.12 , pp. 419-432
    • Kim, W.1    Kang, K.2
  • 82
    • 0035986223 scopus 로고    scopus 로고
    • Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design
    • Brömme, D. and Kaleta, J. Thiol-dependent cathepsins: Pathophysiological implications and recent advances in inhibitor design. Curr Pharm Des 2002, 8: 1639-58.
    • (2002) Curr Pharm Des , vol.8 , pp. 1639-1658
    • Brömme, D.1    Kaleta, J.2
  • 83
    • 0036260967 scopus 로고    scopus 로고
    • Thiol-dependent enzymes and their inhibitors: A review
    • Leung-Toung, R., Li, W., Tam, T.F. et al. Thiol-dependent enzymes and their inhibitors: A review. Curr Med Chem 2002, 9: 879-1002.
    • (2002) Curr Med Chem , vol.9 , pp. 879-1002
    • Leung-Toung, R.1    Li, W.2    Tam, T.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.